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Journal Articles Nucleic Acids Research Year : 2023

DisProt in 2024: improving function annotation of intrinsically disordered proteins

Vasileios Sagris
  • Function : Author
Vasilis Promponas
  • Function : Author
Anastasia Chasapi
  • Function : Author
Erzsébet Fichó
  • Function : Author
Galo Balatti
  • Function : Author
Gustavo Parisi
  • Function : Author
Martín González Buitrón
  • Function : Author
Gabor Erdos
  • Function : Author
Matyas Pajkos
  • Function : Author
Zsuzsanna Dosztányi
  • Function : Author
Laszlo Dobson
  • Function : Author
Alessio Del Conte
  • Function : Author
Damiano Clementel
  • Function : Author
Edoardo Salladini
  • Function : Author
Emanuela Leonardi
  • Function : Author
Fatemeh Kordevani
  • Function : Author
Hamidreza Ghafouri
  • Function : Author
Luiggi Ku
  • Function : Author
Alexander Miguel Monzon
  • Function : Author
Carlo Ferrari
  • Function : Author
Zsófia Kálmán
  • Function : Author
Juliet Nilsson
  • Function : Author
Jaime Santos
  • Function : Author
Carlos Pintado-Grima
  • Function : Author
Salvador Ventura
  • Function : Author
Veronika Ács
  • Function : Author
Rita Pancsa
  • Function : Author
Mariane Goncalves Kulik
  • Function : Author
Miguel Andrade-Navarro
  • Function : Author
Pedro José Barbosa Pereira
  • Function : Author
Philippe Le Mercier
  • Function : Author
Julian Bergier
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Peter Tompa
  • Function : Author
Tamas Lazar
  • Function : Author
Damiano Piovesan
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  • PersonId : 1305736

Abstract

DisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements, including a broader representation of functions and an enhanced curation process. These improvements aim to increase both the quality of annotations and their coverage at the sequence level. Higher coverage has been achieved by adopting additional evidence codes. Quality of annotations has been improved by systematically applying Minimum Information About Disorder Experiments (MIADE) principles and reporting all the details of the experimental setup that could potentially influence the structural state of a protein. The DisProt database now includes new thematic datasets and has expanded the adoption of Gene Ontology terms, resulting in an extensive functional repertoire which is automatically propagated to UniProtKB. Finally, we show that DisProt's curated annotations strongly correlate with disorder predictions inferred from AlphaFold2 pLDDT (predicted Local Distance Difference Test) confidence scores. This comparison highlights the utility of DisProt in explaining apparent uncertainty of certain well-defined predicted structures, which often correspond to folding-upon-binding fragments. Overall, DisProt serves as a comprehensive resource, combining experimental evidence of disorder information to enhance our understanding of intrinsically disordered proteins and their functional implications.
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hal-04278012 , version 1 (09-11-2023)

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Maria Cristina Aspromonte, Maria Victoria Nugnes, Federica Quaglia, Adel Bouharoua, Vasileios Sagris, et al.. DisProt in 2024: improving function annotation of intrinsically disordered proteins. Nucleic Acids Research, In press, ⟨10.1093/nar/gkad928⟩. ⟨hal-04278012⟩
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